{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Mizrak A"],"funding":["U.S. Department of Health &amp; Human Services | NIH | National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["5807"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6925294"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(1)"],"pubmed_abstract":["Transient interactions between the anaphase-promoting complex/cyclosome (APC/C) and its activator subunit Cdc20 or Cdh1 generate oscillations in ubiquitylation activity necessary to maintain the order of cell cycle events. Activator binds the APC/C with high affinity and exhibits negligible dissociation kinetics in vitro, and it is not clear how the rapid turnover of APC/C-activator complexes is achieved in vivo. Here, we describe a mechanism that controls APC/C-activator interactions based on the availability of substrates. We find that APC/C-activator dissociation is stimulated by abundant cellular polyanions such as nucleic acids and polyphosphate. Polyanions also interfere with substrate ubiquitylation. However, engagement with high-affinity substrate blocks the inhibitory effects of p"],"journal":["Nature communications"],"pubmed_title":["Polyanions provide selective control of APC/C interactions with the activator subunit."],"pmcid":["PMC6925294"],"funding_grant_id":["R35-GM118053","R35 GM118053"],"pubmed_authors":["Mizrak A","Morgan DO"],"additional_accession":[]},"is_claimable":false,"name":"Polyanions provide selective control of APC/C interactions with the activator subunit.","description":"Transient interactions between the anaphase-promoting complex/cyclosome (APC/C) and its activator subunit Cdc20 or Cdh1 generate oscillations in ubiquitylation activity necessary to maintain the order of cell cycle events. Activator binds the APC/C with high affinity and exhibits negligible dissociation kinetics in vitro, and it is not clear how the rapid turnover of APC/C-activator complexes is achieved in vivo. Here, we describe a mechanism that controls APC/C-activator interactions based on the availability of substrates. We find that APC/C-activator dissociation is stimulated by abundant cellular polyanions such as nucleic acids and polyphosphate. Polyanions also interfere with substrate ubiquitylation. However, engagement with high-affinity substrate blocks the inhibitory effects of p","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Dec","modification":"2025-04-18T18:40:35.644Z","creation":"2020-05-22T00:09:39Z"},"accession":"S-EPMC6925294","cross_references":{"pubmed":["31862931"],"doi":["10.1038/s41467-019-13864-1"]}}